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Database: UniProt/TrEMBL
Entry: H2K393_STRHJ
LinkDB: H2K393_STRHJ
Original site: H2K393_STRHJ 
ID   H2K393_STRHJ            Unreviewed;       512 AA.
AC   H2K393;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   22-NOV-2017, entry version 39.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=SHJG_2641 {ECO:0000313|EMBL:AEY87915.1};
OS   Streptomyces hygroscopicus subsp. jinggangensis (strain 5008).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1133850 {ECO:0000313|EMBL:AEY87915.1, ECO:0000313|Proteomes:UP000007170};
RN   [1] {ECO:0000313|Proteomes:UP000007170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5008 {ECO:0000313|Proteomes:UP000007170};
RA   Wu H., Bai L.;
RT   "Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis
RT   5008.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP003275; AEY87915.1; -; Genomic_DNA.
DR   RefSeq; WP_014671255.1; NC_017765.1.
DR   ProteinModelPortal; H2K393; -.
DR   STRING; 1133850.SHJG_2641; -.
DR   EnsemblBacteria; AEY87915; AEY87915; SHJG_2641.
DR   KEGG; shy:SHJG_2641; -.
DR   PATRIC; fig|1133850.20.peg.3099; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000007170; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3260.10; -; 2.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007170};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AEY87915.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007170}.
FT   DOMAIN      299    414       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    210    210       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     208    208       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     230    230       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     374    374       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   512 AA;  55043 MW;  DBD10EE3DAB5F1B9 CRC64;
     MLLTRLAQVS REVAATAARS RKIALLAELF RDAEADDVPI VIPYLAGRLP QGRLGVGWKV
     LGRPVPPAAE PSLTVREVDA RLTGLGKVSG PGSQAERTRI VGELMGAATE EEQRFLLGLL
     TGEVRQGALD AVAVEGLARA TGADPADVRR AVMLAGSLQT VAQALLGEGP GSLDRFRLTV
     GRPVLPMLAH SASSVAEAVE KLGACAVEEK LDGIRVQVHR DGDTVRIHTR TLDDITGRLP
     EVTSAALELG GERFILDGEV ISFDAAGRPR SFQETAGRVG SRTDVARAAG QTPVSPVFFD
     ALSVDGRDLL DLPFAERHAE LARLVPEPMR VRRTVASGPE DIPEAERFLA DTLARGHEGV
     VVKALDAPYS AGRRGAAWLK VKPVHTLDLV VLAAEWGHGR RTGKLSNLHL GARTPDGGFA
     MLGKTFKGMT DAMLAWQTER LKELAVEDNG WVVRVRPELV VEIAYDGLQR STRYPAGVTL
     RFARVVRYRE DKRPEEADTV EALLAAHPEV SP
//
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